English   español  
Por favor, use este identificador para citar o enlazar a este item: http://hdl.handle.net/10261/112095
COMPARTIR / IMPACTO:
Estadísticas
logo share SHARE logo core CORE   Add this article to your Mendeley library MendeleyBASE

Visualizar otros formatos: MARC | Dublin Core | RDF | ORE | MODS | METS | DIDL
Exportar a otros formatos:
Título

AMP-activated protein kinase: structure and regulation.

AutorSanz, Pascual
Palabras claveAMP-activated protein kinase
Snf1
LKB1
CaMKK
Phosphatase
Fecha de publicaciónoct-2008
EditorBentham Science Publishers
CitaciónCurrent Protein and Peptide Science 9(5):478-92. (2008)
ResumenMammalian AMP-activated protein kinase (AMPK) is a serine/threonine protein kinase that acts as a sensor of cellular energy status. It is activated by a large variety of cellular stresses that increase cellular AMP and decrease ATP levels and also by physiological stimuli, such as muscle contraction, or by hormones such as leptin and adiponectin. AMPK modulates multiple metabolic pathways. As a result, it has become a target for the development of new drugs for the treatment of type II diabetes, obesity or even cancer. In fact, it has been recently reported that drugs used in the treatment of diabetes, such as metformin and thiazolidinediones (TZDs), exert their beneficial effects through the activation of AMPK. AMPK is a heterotrimeric complex composed of a catalytic subunit (AMPK-) and two regulatory subunits (AMPK- and AMPK-). Functional orthologues of this kinase complex are found throughout eukaryotic kingdom, from yeast to humans, indicating that the function of this complex is evolutionarily conserved. This review summarizes the recent studies on the structure and regulation of the AMPK heterotrimeric complex.
Descripción15 páginas, 5 figuras, 3 tablas
Versión del editorhttp://dx.doi.org/10.2174/138920308785915254
URIhttp://hdl.handle.net/10261/112095
DOI10.2174/138920308785915254
ISSN1389-2037
E-ISSN1875-5550
Aparece en las colecciones: (IBV) Artículos
Ficheros en este ítem:
Fichero Descripción Tamaño Formato  
2008 Curr Protein Pept Sci 9-478.pdf319,65 kBAdobe PDFVista previa
Visualizar/Abrir
Mostrar el registro completo
 

Artículos relacionados:


NOTA: Los ítems de Digital.CSIC están protegidos por copyright, con todos los derechos reservados, a menos que se indique lo contrario.